ID   CYB5_CANTR              Reviewed;         129 AA.
AC   Q874I5;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Cytochrome b5;
GN   Name=Cytb5;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=14532053; DOI=10.1128/aem.69.10.5983-5991.2003;
RA   Craft D.L., Madduri K., Eshoo M., Wilson R.;
RT   "Identification and characterization of the CYP52 family of Candida
RT   tropicalis ATCC 20336, important for the conversion of fatty acids and
RT   alkanes to alpha,omega-dicarboxylic acids.";
RL   Appl. Environ. Microbiol. 69:5983-5991(2003).
CC   -!- FUNCTION: Membrane bound hemoprotein which function as an electron
CC       carrier for several membrane bound oxygenases. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. {ECO:0000305}.
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DR   EMBL; AY230508; AAO73962.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q874I5; -.
DR   SMR; Q874I5; -.
DR   VEuPathDB; FungiDB:CTMYA2_059140; -.
DR   VEuPathDB; FungiDB:CTRG_05068; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.120.10; -; 1.
DR   InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR   InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SMART; SM01117; Cyt-b5; 1.
DR   SUPFAM; SSF55856; SSF55856; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   3: Inferred from homology;
KW   Electron transport; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..129
FT                   /note="Cytochrome b5"
FT                   /id="PRO_0000166028"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          8..84
FT                   /note="Cytochrome b5 heme-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         43
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
FT   BINDING         67
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00279"
SQ   SEQUENCE   129 AA;  14260 MW;  1E29522B41E10762 CRC64;
     MTDTDTTTTI YTHEEVAQHT THDDLWVILN GKVYNISNYI DEHPGGEEVI LDCAGTDATE
     AFDDIGHSDE AHEILEKLYI GNLKGAKIVE AKHAQSFSTE EDSGINFPLI AVGVFLAAFG
     VYYYKTNFA